ArticleJournal of molecular biology2010
Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.
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Who cites it
72 citing papers in PubMed, 1 synthesis or guideline pooled it, 175 citations in OpenAlex.
- Vitamin D-regulated Gene Expression Profiles: Species-specificity and Cell-specific Effects on Metabolism and Immunity.Endocrinology · 2021Pooled it
- Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026Article
- The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.Drug metabolism and disposition: the biological fate of chemicals · 2026Review
- Vitamin D as a cellular endocrine system: Tissue-specific microcircuits, immune reprogramming, and metabolic resistance.iScience · 2026Review
- Review
- Metabolic Interactions of Side-chain Extended and Unsaturated Vitamin D Analogs with Cytochrome P450 Enzymes: Integrating Theoretical and Experimental Approaches.Biomolecules · 2025Article
- An insight into the draft genome of the Oriental rat flea, Xenopsylla cheopis, together with its Wolbachia endosymbiont.BMC genomics · 2025Article
- The impact of inducible-whole body or intestine-specific Cyp24a1 gene knockout on vitamin D metabolism in mice.The Journal of steroid biochemistry and molecular biology · 2025Article
- Molecular dynamics, docking and quantum calculations reveal conformational changes influenced by CYP271A amino acid mutations related to cerebrotendinous xanthomatosis.Scientific reports · 2025Article
- Article
- Hepatocyte vitamin D receptor functions as a nutrient sensor that regulates energy storage and tissue growth in zebrafish.Cell reports · 2024Article
- Article
- Induction of AHR Signaling in Response to the Indolimine Class of Microbial Stress Metabolites.Metabolites · 2023Article
- USP11-mediated LSH deubiquitination inhibits ferroptosis in colorectal cancer through epigenetic activation of CYP24A1.Cell death & disease · 2023Article
- Endogenous Tryptophan-Derived Ah Receptor Ligands are Dissociated from CYP1A1/1B1-Dependent Negative-Feedback.International journal of tryptophan research : IJTR · 2023Article
- The α- and β-Subunit Boundary at the Stem of the Mushroom-Like αApplied and environmental microbiology · 2022Article
- In Silico Prediction of the Metabolic Resistance of Vitamin D Analogs against CYP3A4 Metabolizing Enzyme.International journal of molecular sciences · 2022Article
- Therapeutic Potential of a Novel Vitamin DBiomolecules · 2022Article
- Characterization of a Cleavable Fusion of Human CYP24A1 with Adrenodoxin Reveals the Variable Role of Hydrophobics in Redox Partner Binding.Biochemistry · 2022Article
- The Role of Cytochrome P450 Enzymes in COVID-19 Pathogenesis and Therapy.Frontiers in pharmacology · 2022Review
12 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome P450 (CYP) 24A1 catalyzes the side-chain oxidation of the hormonal form of vitamin D. Expression of CYP24A1 is up-regulated to attenuate vitamin D signaling associated with calcium homeostasis and cellular growth processes. The development of therapeutics for disorders linked to vitamin D insufficiency would be greatly facilitated by structural knowledge of CYP24A1. Here, we report the crystal structure of rat CYP24A1 at 2.5 A resolution. The structure exhibits an open cleft leading to the active-site heme prosthetic group on the distal surface that is likely to define the path of substrate access into the active site. The entrance to the cleft is flanked by conserved hydrophobic residues on helices A' and G', suggesting a mode of insertion into the inner mitochondrial membrane. A docking model for 1alpha,25-dihydroxyvitamin D(3) binding in the open form of CYP24A1 that clarifies the structural determinants of secosteroid recognition and validates the predictive power of existing homology models of CYP24A1 is proposed. Analysis of CYP24A1's proximal surface identifies the determinants of adrenodoxin recognition as a constellation of conserved residues from helices K, K'', and L that converge with an adjacent lysine-rich loop for binding the redox protein. Overall, the CYP24A1 structure provides the first template for understanding membrane insertion, substrate binding, and redox partner interaction in mitochondrial P450s.
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